The MAP kinase JNK‐1 of <i>Caenorhabditis elegans</i>: Location, activation, and influences over temperature‐dependent insulin‐like signaling, stress responses, and fitness

Wolf, M.; Nunes, Frank; Henkel, Arne; Heinick, Alexander; Paul, Rüdiger J.

doi:10.1002/jcp.21269

Cited by 53 publications

(56 citation statements)

References 46 publications

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“…55 sod-2 and sod-1 are highly expressed during normal development, while sod-3 and sod-5 are minor isoforms whose expression is increased in the diapausal dauer larva stage. 7,13,54,56 C. elegans also possesses three genes encoding catalases, ctl-3, ctl-1 and ctl-2, arranged in a tandem array. 9 Six recent reports from five independent research groups have tested the effects of manipulating sod gene expression, with largely consistent results.…”

Section: Manipulation Of C Elegans Antioxidant Enzyme Genesmentioning

confidence: 99%

Antioxidant defense and aging inC. elegans: Is the oxidative damage theory of aging wrong?

Gems¹,

Doonan²

2009

Cell Cycle

236

173

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Section: Manipulation Of C Elegans Antioxidant Enzyme Genesmentioning

confidence: 99%

Antioxidant defense and aging inC. elegans: Is the oxidative damage theory of aging wrong?

Gems¹,

Doonan²

2009

Cell Cycle

236

173

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“…Given that dauer formation is also regulated by the IGF-1-signaling pathway, it would be reasonable to predict that treatment with PUGNAc might also act through the IGF-1-signaling pathway to regulate dauer formation in C. elegans. To test the capacity of PUGNAc to activate the IGF-1-signaling pathway, we monitored the activity of the forkhead (FOXO) transcription factor DAF-16 (which is regulated by the IGF-1-signaling pathway) using daf-16::GFP transgenic worms that had been used previously for this purpose (28,29). When placed on 0.5 mM PUGNAc, these transgenic worms showed no change in the nuclear localization of DAF-16::GFP (Fig.…”

Section: Inhibition Of O-glcnacase Enhances the Frequency Of Dauer Fomentioning

confidence: 99%

Regulation of Dauer Formation by O-GlcNAcylation in Caenorhabditis elegans

Lee

Kim

Lee

et al. 2010

Journal of Biological Chemistry

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Modification of proteins at serine or threonine residues with N-acetylglucosamine, termed O-GlcNAcylation, plays an important role in most eukaryotic cells. To understand the molecular mechanism by which O-GlcNAcylation regulates the entry of Caenorhabditis elegans into the non-aging dauer state, we performed proteomic studies using two mutant strains: the O-GlcNAc transferase-deficient ogt-1(ok430) strain and the O-GlcNAcase-defective oga-1(ok1207) strain. In the presence of the dauer pheromone daumone, ogt-1 showed suppression of dauer formation, whereas oga-1 exhibited enhancement of dauer formation. Consistent with these findings, treatment of wild-type N2 worms with low concentrations of daumone and the O-GlcNAcase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-Nphenylcarbamate (PUGNAc) enhanced dauer formation, which was dependent on intact O-GlcNAcylation metabolism. We also found that the treatment of daumone enhanced O-GlcNAcylation in vivo. Seven proteins, identified by coupled two-dimensional electrophoresis/liquid chromatography-mass spectroscopy (LC-MS) analysis, were differentially expressed in oga-1(ok1207) worms compared with wild-type N2 worms. The identities of these proteins suggest that OGlcNAcylation influences stress resistance, protein folding, and mitochondrial function. Using O-GlcNAc labeling with fluorescent dye combined with two-dimensional electrophoresis/LC-MS analysis, we also identified five proteins that were differentially O-GlcNAcylated during dauer formation. Analysis of these candidate O-GlcNAcylated proteins suggests that O-GlcNAcylation may regulate cytoskeleton modifications and protein turnover during dauer formation.

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“…Among the three subgroups of MAPKs, p38 kinases and c-Jun N-terminal kinases (JNK) are frequently involved in stress responses of animal cells [8]. C. elegans expresses JNK and JNK-like MAPKs in a tissue-specific way, with JNK-1 and its upstream kinase, the MAP2K JKK-1, expressed only in neuronal cells [9,10]. The signaling pathway of the JNK-like MAPK KGB-1 is composed of MLK-1 (MAP3K), MEK-1 (MAP2K), and KGB-1 [11,12].…”

Section: Introductionmentioning

confidence: 99%

The JNK-Like MAPK KGB-1 ofCaenorhabditis ElegansPromotes Reproduction, Lifespan, and Gene Expressions for Protein Biosynthesis and Germline Homeostasis but Interferes with Hyperosmotic Stress Tolerance

Gerke

Keshet

Mertenskötter

et al. 2014

Cell Physiol Biochem

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Aims: This study focused on the role of the JNK-like MAPK (mitogen-activated protein kinase) KGB-1 (kinase, GLH-binding 1) for osmoprotection and other vital functions. Methods: We mapped KGB-1 expression patterns and determined lifespan, reproduction and survival rates as well as changes in body volume, motility, and GPDH (glycerol-3-phosphate dehydrogenase) activity for glycerol production in wildtype (WT), different signaling mutants (including a kgb-1 deletion mutant, kgb-1∆) and RNAi-treated worms under control and hyperosmotic conditions. KGB-1-mediated gene expressions were studied, for instance, by RNA Sequencing, with the resulting transcriptome data analyzed using orthology-based approaches. Results: Surprisingly, mutation/RNAi of kgb-1 and fos-1 (gene for an AP-1, activator protein 1, element) significantly promoted hyperosmotic resistance, even though hyperosmotic GPDH activity was higher in WT than in kgb-1∆. KGB-1 and moderate hyperosmolarity promoted and severe hyperosmolarity repressed kgb-1, fos-1, and jun-1 (gene for another AP-1 element) expression. Transcriptome profiling revealed, for instance, down-regulated genes for protein biosynthesis and up-regulated genes for membrane transporters in kgb-1∆ and up-regulated genes for GPDH-1 or detoxification in WT, with the latter indicating cellular damage and less effective osmoprotection in WT. Conclusion: KGB-1 promotes reproduction and lifespan and fosters gene expressions for AP-1 elements, protein biosynthesis, and balanced gametogenesis, but inhibits expressions for membrane transporters perhaps in order to control energy consumption. Reduced protein biosyntheses and enhanced membrane transports in kgb-1∆ most likely contribute to the high hyperosmotic tolerance of the mutant by easing the burden of the existing chaperone machinery and promoting regulatory volume increases upon hyperosmotic stress.

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The MAP kinase JNK‐1 of Caenorhabditis elegans: Location, activation, and influences over temperature‐dependent insulin‐like signaling, stress responses, and fitness

Cited by 53 publications

References 46 publications

Antioxidant defense and aging inC. elegans: Is the oxidative damage theory of aging wrong?

Antioxidant defense and aging inC. elegans: Is the oxidative damage theory of aging wrong?

Regulation of Dauer Formation by O-GlcNAcylation in Caenorhabditis elegans

The JNK-Like MAPK KGB-1 ofCaenorhabditis ElegansPromotes Reproduction, Lifespan, and Gene Expressions for Protein Biosynthesis and Germline Homeostasis but Interferes with Hyperosmotic Stress Tolerance

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